Structure of PDB 5t4p Chain C

Receptor sequence
>5t4pC (length=508) Species: 562 (Escherichia coli) [Search protein sequence]
NSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADAMQGEMI
SLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKATGRILEVPVGRGL
LGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAV
DSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKAIYVAIGQKAS
TISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGAAMGEYFRDRG
EDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAR
VNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQI
FLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYREL
AAFSQFASDLDDATRNQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAER
GYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKLKGI
LDSFKATQ
3D structure
PDB5t4p Cryo-EM structures of the autoinhibitedE. coliATP synthase in three rotational states.
ChainC
Resolution7.77 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q200 K201 R376
Catalytic site (residue number reindexed from 1) K172 Q197 K198 R373
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ATP C D170 R171 Q172 T173 G174 K175 T176 A177 F360 G363 I364 R365 A367 Q435 D167 R168 Q169 T170 G171 K172 T173 A174 F357 G360 I361 R362 A364 Q432
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5t4p, PDBe:5t4p, PDBj:5t4p
PDBsum5t4p
PubMed28001127
UniProtP0ABB0|ATPA_ECOLI ATP synthase subunit alpha (Gene Name=atpA)

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